ID Q07MF3_RHOP5 Unreviewed; 331 AA.
AC Q07MF3;
DT 31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE RecName: Full=N-acetyl-gamma-glutamyl-phosphate reductase {ECO:0000256|HAMAP-Rule:MF_01110};
DE Short=AGPR {ECO:0000256|HAMAP-Rule:MF_01110};
DE EC=1.2.1.38 {ECO:0000256|HAMAP-Rule:MF_01110};
DE AltName: Full=N-acetyl-glutamate semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01110};
DE Short=NAGSA dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01110};
GN Name=argC {ECO:0000256|HAMAP-Rule:MF_01110};
GN OrderedLocusNames=RPE_2944 {ECO:0000313|EMBL:ABJ06881.1};
OS Rhodopseudomonas palustris (strain BisA53).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=316055 {ECO:0000313|EMBL:ABJ06881.1};
RN [1] {ECO:0000313|EMBL:ABJ06881.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisA53 {ECO:0000313|EMBL:ABJ06881.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Kim E., Harwood C.S., Oda Y.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisA53.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of N-acetyl-5-
CC glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
CC {ECO:0000256|HAMAP-Rule:MF_01110}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate =
CC H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH; Xref=Rhea:RHEA:21588,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29123, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:57936, ChEBI:CHEBI:58349; EC=1.2.1.38;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01110};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 3/4. {ECO:0000256|HAMAP-
CC Rule:MF_01110}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01110}.
CC -!- SIMILARITY: Belongs to the NAGSA dehydrogenase family. Type 2
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01110}.
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DR EMBL; CP000463; ABJ06881.1; -; Genomic_DNA.
DR AlphaFoldDB; Q07MF3; -.
DR STRING; 316055.RPE_2944; -.
DR KEGG; rpe:RPE_2944; -.
DR eggNOG; COG0002; Bacteria.
DR HOGENOM; CLU_077118_0_0_5; -.
DR OrthoDB; 9801289at2; -.
DR UniPathway; UPA00068; UER00108.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_01110; ArgC_type2; 1.
DR InterPro; IPR023013; AGPR_AS.
DR InterPro; IPR010136; AGPR_type-2.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR NCBIfam; TIGR01851; argC_other; 1.
DR PANTHER; PTHR32338:SF10; N-ACETYL-GAMMA-GLUTAMYL-PHOSPHATE REDUCTASE, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR32338; N-ACETYL-GAMMA-GLUTAMYL-PHOSPHATE REDUCTASE, CHLOROPLASTIC-RELATED-RELATED; 1.
DR Pfam; PF01118; Semialdhyde_dh; 1.
DR SMART; SM00859; Semialdhyde_dh; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS01224; ARGC; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_01110};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571, ECO:0000256|HAMAP-
KW Rule:MF_01110}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01110};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_01110};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01110}.
FT DOMAIN 20..124
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 135
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01110,
FT ECO:0000256|PROSITE-ProRule:PRU10010"
SQ SEQUENCE 331 AA; 35074 MW; A553441DF11EB6D4 CRC64;
MTLSETTRPE GAPRRTGKPN VFVDGAAGTT GLGIRERLGR SNQVTLRQID DDKRKDAAAK
RALMEEVDLV ILCLPDDAAK ETVALIDSMG DAAPKVLDAS TAFRVASDWT YGFPELAPDQ
ADKIRAARKV ANPGCYPTGS IALLRPLVDA GLLPAEYPVT INAVSGYSGG GKAMIAAYEA
GSAPAFELYG LGFEHKHLPE TQFYARLTRR PIFVPSVGSF RQGMLVSVPL HLDTLPGKPG
VADLHAVLDQ RYAGSATVSV APRDGATIAS GKIEPEALNE TNKLELFVFG SDTHRQAVLV
ARLDNLGKGA SGAAVQNMRL MLGLPETPGL D
//
